ID Q88QB2_PSEPK Unreviewed; 425 AA.
AC Q88QB2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Thiolase family protein {ECO:0000313|EMBL:AAN66209.1};
GN OrderedLocusNames=PP_0582 {ECO:0000313|EMBL:AAN66209.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN66209.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN66209.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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DR EMBL; AE015451; AAN66209.1; -; Genomic_DNA.
DR RefSeq; NP_742745.1; NC_002947.4.
DR RefSeq; WP_010951855.1; NC_002947.4.
DR AlphaFoldDB; Q88QB2; -.
DR STRING; 160488.PP_0582; -.
DR PaxDb; 160488-PP_0582; -.
DR GeneID; 83677906; -.
DR KEGG; ppu:PP_0582; -.
DR PATRIC; fig|160488.4.peg.621; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OrthoDB; 1402717at2; -.
DR PhylomeDB; Q88QB2; -.
DR BioCyc; PPUT160488:G1G01-632-MONOMER; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000000556};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 7..274
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 283..425
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 425 AA; 45543 MW; DCCAB6A99C5129C9 CRC64;
MRSTRRVAIL GGNRIPFARS NGAYATASNQ AMLTAALEGL IERYRLHGLR LGEVVAGAVL
KHSRDMNLTR ECVLGSRLSP QTPAYDIQQA CGTGLEAALL VANKIALGQI DCGIAGGVDS
TSDAPIAVNE GLRHILLQAN RGKSLGERLK PFLKLRPHHL KPELPRNSEP RTGLSMGEHC
ERMAHTWRVG RAEQDELALL SHQKLAAAYA EGWQDDLLTP FLSLARDNNL RPDLSLEQLA
RLKPAFDRSG QGTLTAGNST PLTDGASLVL LGSEAWAQQQ GLQVLAYLVD GETAAVDFVT
GREGLLMAPV YAVPRLLARN GLTLQDFDYY EIHEAFAAQV LCTLKAWEDA DYCRERLGLE
APLGAIDRSK LNVRGSSLAA GHPFAATGGR ILANLAKLLA TAGKGRGLIS ICAAGGQGVT
VIVER
//
